A novel method for purification of biologically active C-terminal fragment of human recombinant anti-mullerian hormone.

Autor: Rak AY; State Research Institute of Highly Pure Biopreparations, St Petersburg, Russian Federation., Protasov EA; State Research Institute of Highly Pure Biopreparations, St Petersburg, Russian Federation., Trofimov AV; State Research Institute of Highly Pure Biopreparations, St Petersburg, Russian Federation., Pigareva NV; State Research Institute of Highly Pure Biopreparations, St Petersburg, Russian Federation., Ischenko AM; State Research Institute of Highly Pure Biopreparations, St Petersburg, Russian Federation.
Jazyk: angličtina
Zdroj: Biomedical chromatography : BMC [Biomed Chromatogr] 2022 Feb; Vol. 36 (2), pp. e5259. Date of Electronic Publication: 2021 Nov 15.
DOI: 10.1002/bmc.5259
Abstrakt: Anti-mullerian hormone (AMH) is one of the least studied members of transforming growth factor beta superfamily showing pro-apoptotic activity against cells positive for hormone type II receptor overexpressed by malignant cells in many cancer cases. Here, we propose an improved method for isolation of recombinant C-terminal AMH fragment (C-rAMH) to obtain homogeneous preparations of this protein with high biological activity. In contrast to our previously developed C-rAMH purification technology based on reversed-phase HPLC, the key stage of the new approach is hydrophobic interaction chromatography using Toyopearl Butyl-650S resin performed under more benign conditions. This modification of the previously developed method allowed highly purified C-rAMH to be obtained that is characterized by twice the specificity estimated as the ability to bind to the recombinant analog of AMH type II receptor and by significantly higher biological activity, that is, the ability to induce the death of target cells. Thus, we made the purification technology even more cost-effective and suitable for the production of drug forms based on C-rAMH.
(© 2021 John Wiley & Sons, Ltd.)
Databáze: MEDLINE
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